2011 Fiscal Year Final Research Report
Single molecule reaction analysis of P-types ATPase using electrochemical fast-scanning atomic force microscopy
Project/Area Number |
22770148
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Single-year Grants |
Research Field |
Biophysics
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Research Institution | University of Tsukuba |
Principal Investigator |
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Project Period (FY) |
2010 – 2011
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Keywords | P 型ATPase / SERCA / Na+-Pump / 高速AFM / 一分子解析 |
Research Abstract |
Ion pumps transport specific cationic ion across the biomembrane against a concentration gradient through the energy obtained from ATP hydrolysis. Recent progresses in crystallographic study of sarcoplasmic reticulum Ca^<2+>-ATPase (SERCA), which is one of the best-characterized P-type ATPases, allow us to discuss the transport mechanisms involving dynamical structural changes of P-type ATPases. In this study, we constructed a novel method to analyze molecular reaction of P-type ATPase at a single molecular level and real time scale using a newly developed fast-scanning atomic force microscopy. Using the system, we succeeded to observe single molecule of SERCA and plasma membrane sodium pump act as a pumping machine by direct detection of their repeatedly up-and-down conformational changes.
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